3O5Z

Crystal structure of the SH3 domain from p85beta subunit of phosphoinositide 3-kinase (PI3K)

Summary for 3O5Z

• Entry DOI: 10.2210/pdb3o5z/pdb
• Descriptor: Phosphatidylinositol 3-kinase regulatory subunit beta, CHLORIDE ION, (4S)-2-METHYL-2,4-PENTANEDIOL, ... (4 entities in total)
• Functional Keywords: src homology 3 domain, protein binding
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 2
• Total formula weight: 19811.33

Authors

Chen, S.,Xiao, Y.,Ponnusamy, R.,Tan, J.,Lei, J.,Hilgenfeld, R. (deposition date: 2010-07-28, release date: 2011-08-10, Last modification date: 2024-10-30)

Primary citation

Chen, S.,Xiao, Y.,Ponnusamy, R.,Tan, J.,Lei, J.,Hilgenfeld, R.
X-ray structure of the SH3 domain of the phosphoinositide 3-kinase p85 beta subunit
Acta Crystallogr.,Sect.F, 67:1328-1333, 2011

PubMed Abstract: Src-homology 3 (SH3) domains are involved in extensive protein-protein interactions and constitute key elements of intracellular signal transduction. Three-dimensional structures have been reported for SH3 domains of various proteins, including the 85 kDa regulatory subunit (p85) of phosphoinositide 3-kinase. However, all of the latter structures are of p85 isoform α and no crystal structure of the SH3 domain of the equally important isoform β has been reported to date. In this structural communication, the recombinant production, crystallization and X-ray structure determination at 2.0 Å resolution of the SH3 domain of human p85β is described. The structure reveals a compact β-barrel fold very similar to that of p85α. However, binding studies with two classes of proline-rich ligand peptides demonstrate that the ligand-binding specificity differs slightly between the SH3 domains of human p85β and p85α, despite their high structural similarity.

PubMed: 22102226
DOI: 10.1107/S1744309111031691

Experimental method

X-RAY DIFFRACTION (2.01 Å)